Literature DB >> 12417049

Protein folding in the post-genomic era.

Jeannine M Yon1.   

Abstract

Protein folding is a topic of fundamental interest since it concerns the mechanisms by which the genetic message is translated into the three-dimensional and functional structure of proteins. In these post-genomic times, the knowledge of the fundamental principles are required in the exploitation of the information contained in the increasing number of sequenced genomes. Protein folding also has practical applications in the understanding of different pathologies and the development of novel therapeutics to prevent diseases associated with protein misfolding and aggregation. Significant advances have been made ranging from the Anfinsen postulate to the "new view" which describes the folding process in terms of an energy landscape. These new insights arise from both theoretical and experimental studies. The problem of folding in the cellular environment is briefly discussed. The modern view of misfolding and aggregation processes that are involved in several pathologies such as prion and Alzheimer diseases. Several approaches of structure prediction, which is a very active field of research, are described.

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Year:  2002        PMID: 12417049      PMCID: PMC6740087          DOI: 10.1111/j.1582-4934.2002.tb00511.x

Source DB:  PubMed          Journal:  J Cell Mol Med        ISSN: 1582-1838            Impact factor:   5.310


  7 in total

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Authors:  Vijay M Krishnamurthy; George K Kaufman; Adam R Urbach; Irina Gitlin; Katherine L Gudiksen; Douglas B Weibel; George M Whitesides
Journal:  Chem Rev       Date:  2008-03       Impact factor: 60.622

2.  Human stefin B normal and patho-physiological role: molecular and cellular aspects of amyloid-type aggregation of certain EPM1 mutants.

Authors:  Mira Polajnar; Slavko Ceru; Nataša Kopitar-Jerala; Eva Zerovnik
Journal:  Front Mol Neurosci       Date:  2012-08-24       Impact factor: 5.639

3.  A staphylococcal anti-sigma factor possesses a single-domain, carries different denaturant-sensitive regions and unfolds via two intermediates.

Authors:  Debabrata Sinha; Rajkrishna Mondal; Avisek Mahapa; Keya Sau; Rajagopal Chattopadhyaya; Subrata Sau
Journal:  PLoS One       Date:  2018-04-05       Impact factor: 3.240

4.  Proteomic profiling of proteins in the dorsal horn of the spinal cord in dairy cows with chronic lameness.

Authors:  Daniel Herzberg; Pablo Strobel; Heine Müller; Constanza Meneses; Marianne Werner; Hedie Bustamante
Journal:  PLoS One       Date:  2020-01-28       Impact factor: 3.240

5.  Structural characterization of the thermal unfolding pathway of human VEGFR1 D2 domain.

Authors:  Donatella Diana; Rossella Di Stasi; Sara García-Viñuales; Lucia De Rosa; Carla Isernia; Gaetano Malgieri; Danilo Milardi; Luca D D'Andrea; Roberto Fattorusso
Journal:  FEBS J       Date:  2021-11-18       Impact factor: 5.622

Review 6.  Folding by numbers: primary sequence statistics and their use in studying protein folding.

Authors:  Brent Wathen; Zongchao Jia
Journal:  Int J Mol Sci       Date:  2009-04-08       Impact factor: 6.208

7.  Implications from a network-based topological analysis of ubiquitin unfolding simulations.

Authors:  Arun Krishnan; Alessandro Giuliani; Joseph P Zbilut; Masaru Tomita
Journal:  PLoS One       Date:  2008-05-14       Impact factor: 3.240

  7 in total

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